Developing Functional Mimics of Active Sites of Metalloenzymes Involved in Carbohydrate Binding and Transformation

dc.contributor.advisorMusie, Ghezai T.
dc.contributor.authorStewart, Christopher David
dc.contributor.committeeMemberKurtz, Donald M.
dc.contributor.committeeMemberTonzetich, Zachary J.
dc.contributor.committeeMemberChen, Banglin
dc.creator.orcidhttps://orcid.org/0000-0003-3280-5957
dc.date.accessioned2024-03-08T15:43:15Z
dc.date.available2024-03-08T15:43:15Z
dc.date.issued2018
dc.descriptionThis item is available only to currently enrolled UTSA students, faculty or staff. To download, navigate to Log In in the top right-hand corner of this screen, then select Log in with my UTSA ID.
dc.description.abstractCarbohydrates comprise the most abundant class of organic molecules in the biosphere and find crucial roles in a vast number of biological functions. Despite their overwhelming importance, the study of metalloenzymes involved in carbohydrate metabolism such as Xylose/Glucose isomerase (XGI) using synthetic models remains largely unexplored. Towards the goal of expanding the scientific knowledge surrounding the interaction and reactivity of carbohydrates with metal complexes, new biologically relevant transition metal complexes as carbohydrate binding models have been synthesized and fully characterized using several techniques including single crystal X-ray crystallography. Several new ligands were developed to provide a coordination environment around the metal centers very similar to those found in the active site of metalloenzymes. Nearly all of the metal complexes of these new ligands were found to be soluble in common polar solvents including water. The binding of substrates such as D-mannose, D-glucose, D-xylose and xylitol with the water-soluble complexes in different reaction conditions were investigated. The metal complexes showed coordination ability towards the applied substrates. Even in the presence of stoichiometric excess of the substrates, the complexes form only 1:1 (complex/substrate) molar ratio species in solution. Apparent binding constants, pKapp, values between the complexes and the substrates were determined and specific mode of substrate binding has been proposed. Syntheses, characterizations and detailed substrate binding study using spectroscopic techniques and single crystal X-ray diffraction are reported.
dc.description.departmentChemistry
dc.format.extent211 pages
dc.format.mimetypeapplication/pdf
dc.identifier.isbn9780438739413
dc.identifier.urihttps://hdl.handle.net/20.500.12588/5629
dc.languageen
dc.subjectBinding constants
dc.subjectCarbohydrates
dc.subjectMetal complex
dc.subjectMetalloenzymes
dc.subjectMonosaccharides
dc.subjectSugar–metal complex interaction
dc.subject.classificationChemistry
dc.subject.classificationInorganic chemistry
dc.subject.classificationBiochemistry
dc.titleDeveloping Functional Mimics of Active Sites of Metalloenzymes Involved in Carbohydrate Binding and Transformation
dc.typeThesis
dc.type.dcmiText
dcterms.accessRightspq_closed
thesis.degree.departmentChemistry
thesis.degree.grantorUniversity of Texas at San Antonio
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy

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